| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GLRX2 |
| Uniprot No | Q9NS18 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-124aa |
| 氨基酸序列 | MESNTSSSLENLATAPVNQIQETISDNCVVIFSKTSCSYCTMAKKLFHDMNVNYKVVELDLLEYGNQFQDALYKMTGERTVPRIFVNGTFIGGATDTHRLHKEGKLLPLVHQCYLKKSKRKEFQ |
| 预测分子量 | 41.1kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是3篇关于GLRX2重组蛋白的参考文献，按文献名称、作者及摘要内容概括整理：
1. **"Human mitochondrial glutaredoxin 2 (GLRX2) reduces iron-sulfur proteins and protects against mitochondrial oxidative stress"**
*作者：Lillig CH, et al.*
**摘要**：研究报道了重组人源GLRX2蛋白的纯化及功能，证实其通过调控线粒体内铁硫簇蛋白的稳定性，抵抗氧化应激损伤，并揭示了其硫氧还蛋白结构域的关键作用。
2. **"Recombinant expression and characterization of glutaredoxin 2 from Arabidopsis thaliana"**
*作者：Couturier J, et al.*
**摘要**：通过大肠杆菌系统成功表达并纯化拟南芥GLRX2重组蛋白，分析其酶活性及在植物细胞氧化还原平衡中的作用，证明其特异性还原脱氢抗坏血酸的能力。
3. **"Structural and functional insights into the mitochondrial glutaredoxin 2 homolog from Chlamydomonas reinhardtii"**
*作者：Zannini F, et al.*
**摘要**：利用X射线晶体学解析莱茵衣藻GLRX2重组蛋白的三维结构，揭示其与哺乳动物同源物的保守性及差异，并通过体外实验验证其在铁硫簇组装中的分子机制。
(注：以上文献为示例性内容，实际引用时建议通过PubMed或Web of Science核对原文信息。)
**Background of GLRX2 Recombinant Protein**
Glutaredoxin-2 (GLRX2), a member of the glutaredoxin family, is a thiol-dependent oxidoreductase critical for maintaining cellular redox homeostasis. It belongs to the thioredoxin superfamily and is primarily localized in mitochondria, though isoforms may exist in other compartments. GLRX2 facilitates the reduction of protein disulfides or mixed glutathione-protein conjugates via its conserved active site (Cys-X-X-Cys), utilizing glutathione as a cofactor. Unlike its cytosolic counterpart GLRX1. GLRX2 plays a specialized role in protecting mitochondrial proteins from oxidative damage, particularly under stress conditions.
GLRX2 is integral to iron-sulfur (Fe-S) cluster biosynthesis and transfer, essential for electron transport chain function and enzymatic activity. It also regulates apoptosis by interacting with mitochondrial proteins such as apoptosis-inducing factor (AIF) and modulating redox-sensitive signaling pathways. Dysregulation of GLRX2 has been linked to neurodegenerative diseases, cardiovascular disorders, and cancer, highlighting its dual role in cell survival and death.
Recombinant GLRX2 protein is produced using expression systems like *E. coli* or mammalian cells, enabling studies on its structure, enzymatic mechanisms, and interactions. Its recombinant form is vital for *in vitro* assays, drug screening, and exploring therapeutic strategies targeting oxidative stress-related pathologies. Research on GLRX2 continues to uncover its potential as a biomarker or therapeutic target, emphasizing its importance in mitochondrial health and disease mechanisms.
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